Species | Paraprevotella sp900546665 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella sp900546665 | |||||||||||
CAZyme ID | MGYG000000559_01031 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 24804; End: 26033 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13528 | Glyco_trans_1_3 | 9.00e-27 | 1 | 328 | 1 | 316 | Glycosyl transferase family 1. |
cd03785 | GT28_MurG | 7.44e-08 | 2 | 319 | 1 | 307 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AND20562.1 | 3.24e-166 | 1 | 359 | 1 | 359 |
QJR76573.1 | 6.52e-166 | 1 | 359 | 1 | 359 |
QUT84114.1 | 6.52e-166 | 1 | 359 | 1 | 359 |
QJR55086.1 | 6.52e-166 | 1 | 359 | 1 | 359 |
QJR72500.1 | 6.52e-166 | 1 | 359 | 1 | 359 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000056 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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